{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070885/BL21DE3_ga0523514_proteins_annotation.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070885/checksum.txt"],"Xml":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070885/Smear-gel-band-at-high-position.xml","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070885/2-batches_NuoEF-Strep_samples-pooled.xml","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070885/Sharp-gel-band-at_low-position.xml","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070885/2-batches_HydA-Strep_samples-pooled.xml"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070885/Sharp-gel-band-at_low-position.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070885/2-batches_HydA-Strep_sample-pooled.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070885/Smear-gel-band-at-high-position.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070885/2-batches_NuoEF-Strep_samples-pooled.raw"],"Mgf":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070885/Sharp-gel-band-at_low-position.mgf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070885/2-batches_NuoEF-Strep_samples-pooled.mgf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070885/2-batches_HydA-Strep_sample-pooled.mgf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070885/Smear-gel-band-at-high-position.mgf"],"Fasta":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070885/NuoEF-Strep_BL21DE3_ga0523514_proteins.fasta","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070885/HydA-Strep_HydGXEF_BL21DE3_ga0523514_proteins.fasta","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070885/Strep-HydA_NuoEF_HydGXEF_BL21DE3_ga0523514_proteins.fasta"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["momalley@ucsb.edu"],"submitter":["Bo Zhang"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"software":["Not available"],"submitter_keywords":["Lc-ms/ms"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD070885"],"sample_protocol":["Hyd-Strep protein (C. churrovis matured Hyd, MycoCosm protein ID 243125) was co-expressed with Shewanella oneidensis MR-1 HydGXEF in E. coli BL21(DE3)ΔiscR, and purified via strep-tactin XT 4flow high capacity resin column. NuoEF-strep protein (C. churrovis matured NuoE [protein ID 454874] and NuoF-Strep [protein ID557447]) was overexpressed in E. coli BL21(DE3)ΔiscR, and purified via strep-tactin superflow high capacity resin column.  Two batches of Hyd-Strep were pooled. Two batches of NuoEF-Strep were pooled. These pooled samples (purified proteins) were precipitated by trichloroacetic acid/acetone solution, denatured by urea, reduced by DTT, alkylated by iodoacetamide, digested by trypsin/Lys-C mix (Promega #V5073), and cleaned with C18 tips. The eluted peptides were analyzed by LC-MS/MS in Data-Dependent Acquisition (DDA) mode as described in literature (Zhang, et al., Applied and environmental microbiology 87.14 (2021): e02959-20.). Briefly, the LC was a Dionex UltiMate 3000 RSLC system (Thermo Fisher) equipped with a PepMap C18 column (75 μm by 25 cm with a 2-μm pore size; Thermo Scientific). The amount of peptide injected was 1 μg, the flow rate of the mobile phase was 200 μl/min, and the column temperature was 40°C. The mobile phases were 0.1% formic acid (v/v) in water (A) and 0.1% formic acid (v/v) in acetonitrile (B), and they were used in a gradient elution. The concentration of B was decreased from 10 to 8% over 3 min, increased to 46% over 66 min, increased to 99% over 3 min, held at 99% for 2 min, decreased to 2% over 0.5 min, and held at 2% for 15 min. The MS was an Orbitrap Fusion Lumos (Thermo Scientific) operated in DDA mode. MS/MS spectra were acquired with automatic gain control target of 5 × 103, ion filling time of 35 ms, and dynamic exclusion time of 50 s with a 10-ppm mass window.   In addition to the purified protein samples, we also used LC-MS/MS to identify proteins in gel bands. These two gel bands were from the protein sample purified from E. coli BL21(DE3)ΔiscR overexpressing Strep-Hyd, NuoE, NuoF of C. churrovis, and HydGXEF of S. oneidensis MR-1.  These two gel bands were called “Smear gel band at high position” and the “Sharp gel band at low position”. The gel band was cut into pieces and destained by washing in 25 mM NH4HCO3 for 5 min, 50% (v/v) acetonitrile and 25 mM NH4HCO3 in water for 5 min, and 100% acetonitrile. We repeated this step and then washed them in 100 mM NH4HCO3 for 15 min, 100% acetonitrile for 10 min, 100 mM NH4HCO3 for 15 min, 100% acetonitrile for 10 min. The dried gel pieces were reduced by mixed in 100 mM DTT in 50 mM for 90 min at 56°C, spined to remove excess liquid, shrinked in 100% acetonitrile, and alkylated in 55 mM iodoacetamide for 20 min in the dark. The excess liquid was removed and gel pieces were washed with 50 mM NH4HCO3 for 15 min twice, shrinked with 100% acetonitrile, and digested with trypsin in 150 µL of 50 mM NH4HCO3 at 37°C overnight. The digestion reaction was quenched by 6.5 µL formic acid. The peptides were extracted, cleaned with C18 tips, dried, resuspended in 0.1% (v/v) trifluoroacetic acid, and analyzed by LC-MS/MS in DDA mode as described above."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Peptides and proteins were identified from LC-MS/MS data using X!TandemPipeline software, version 0.2.38. The database for the heterologously generated Hyd-Strep sample was a fasta file containing all proteins in E. coli BL21(DE3) predicted by IMG/M and the protein sequences of Hyd-Strep of Caecomyces churrovis, and the protein sequences of HydGXEF of Shewanella oneidensis MR-1.  The database for the heterologously generated NuoEF-Strep sample was a fasta file containing all proteins in E. coli BL21(DE3) predicted by IMG/M and the protein sequences of NuoE and NuoF-Strep of Caecomyces churrovis.  The database for the proteins in two gel bands was a fasta file containing all proteins in E. coli BL21(DE3) predicted by IMG/M and the protein sequences of Strep-Hyd, NuoE, and NuoF of Caecomyces churrovis, and the protein sequences of HydGXEF of Shewanella oneidensis MR-1. The parameter “Fragment ion mass tolerance (monoisotropic)” was set to 0.1. All other parameters were kept at default values."],"omics_type":["Proteomics"],"labhead":["Michelle O'Malley"],"instrument_platform":[""],"labhead_affiliation":["Department of Chemical Engineering, Department of Bioengineering, University of California, Santa Barbara, USA"],"submission_type":["PARTIAL"],"species":["Escherichia Coli"],"submitter_mail":["bozhang@ucsb.edu"],"publication":["Not available"],"submitter_affiliation":["University of California, Santa Barbara"],"submitter_country":["United States"],"additional_accession":[]},"is_claimable":false,"name":"Shotgun proteomics of heterologously generated proteins and proteins in gel bands","description":"We performed shotgun proteomics on the heterolously generated proteins and proteins in gel 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